Surface diffusion of interacting proteins. Effect of concentration on the lateral mobility of adsorbed bovine serum albumin.
Surface diffusion of bovine serum albumin absorbed from aqueous solution to poly(methylmethacrylate) surfaces is significantly hindered by protein-protein lateral interactions. The long-time self diffusion coefficient measured by fluorescence recovery after pattern photobleaching decreases by approximately one order of magnitude as the surface area fraction occupied by protein increases from 0.10 to 0.69. Qualitative features of the surface concentration dependence of the self diffusion coefficient can be described by several recent models for lateral diffusion of interacting species. The mobile fraction is independent of the surface concentration, and both the self diffusion coefficient and the mobile fraction are constant between 15 min and 7 h of adsorption.
Tilton
R D
RD
Department of Chemical Engineering, Stanford University, California 94305-5025.
Gast
A P
AP
Robertson
C R
CR
D000327:Adsorption; D055592:Biophysical Phenomena; D001703:Biophysics; D004058:Diffusion; D008768:Methylmethacrylates; D008956:Models, Chemical; D012710:Serum Albumin, Bovine; D013499:Surface Properties
D008768:Methylmethacrylates; D012710:Serum Albumin, Bovine